3QYT
Diferric bound human serum transferrin
Summary for 3QYT
| Entry DOI | 10.2210/pdb3qyt/pdb |
| Related | 2HAV 4H0W |
| Descriptor | Serotransferrin, FE (III) ION, CARBONATE ION, ... (6 entities in total) |
| Functional Keywords | diferric, human transferrin, intermediate, iron transporter, metal transport |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 76054.66 |
| Authors | |
| Primary citation | Yang, N.,Zhang, H.,Wang, M.,Hao, Q.,Sun, H. Iron and bismuth bound human serum transferrin reveals a partially-opened conformation in the N-lobe Sci Rep, 2:999-999, 2012 Cited by PubMed Abstract: Human serum transferrin (hTF) binds Fe(III) tightly but reversibly, and delivers it to cells via a receptor-mediated endocytosis process. The metal-binding and release result in significant conformational changes of the protein. Here, we report the crystal structures of diferric-hTF (Fe(N)Fe(C)-hTF) and bismuth-bound hTF (Bi(N)Fe(C)-hTF) at 2.8 and 2.4 Å resolutions respectively. Notably, the N-lobes of both structures exhibit unique "partially-opened" conformations between those of the apo-hTF and holo-hTF. Fe(III) and Bi(III) in the N-lobe coordinate to, besides anions, only two (Tyr95 and Tyr188) and one (Tyr188) tyrosine residues, respectively, in contrast to four residues in the holo-hTF. The C-lobe of both structures are fully closed with iron coordinating to four residues and a carbonate. The structures of hTF observed here represent key conformers captured in the dynamic nature of the transferrin family proteins and provide a structural basis for understanding the mechanism of metal uptake and release in transferrin families. PubMed: 23256035DOI: 10.1038/srep00999 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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